ID A0A0Q8F9K4_9GAMM Unreviewed; 498 AA.
AC A0A0Q8F9K4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Lysine 6-aminotransferase {ECO:0000313|EMBL:KRA53277.1};
GN ORFNames=ASD77_00830 {ECO:0000313|EMBL:KRA53277.1};
OS Pseudoxanthomonas sp. Root65.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1736576 {ECO:0000313|EMBL:KRA53277.1, ECO:0000313|Proteomes:UP000051430};
RN [1] {ECO:0000313|EMBL:KRA53277.1, ECO:0000313|Proteomes:UP000051430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root65 {ECO:0000313|EMBL:KRA53277.1,
RC ECO:0000313|Proteomes:UP000051430};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA53277.1, ECO:0000313|Proteomes:UP000051430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root65 {ECO:0000313|EMBL:KRA53277.1,
RC ECO:0000313|Proteomes:UP000051430};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRA53277.1}.
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DR EMBL; LMHA01000001; KRA53277.1; -; Genomic_DNA.
DR RefSeq; WP_055935991.1; NZ_LMHA01000001.1.
DR AlphaFoldDB; A0A0Q8F9K4; -.
DR STRING; 1736576.ASD77_00830; -.
DR OrthoDB; 6188639at2; -.
DR Proteomes; UP000051430; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43206:SF2; 4-AMINOBUTYRATE AMINOTRANSFERASE GABT; 1.
DR PANTHER; PTHR43206; AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KRA53277.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000051430};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRA53277.1}.
SQ SEQUENCE 498 AA; 53713 MW; 3EAFE22F82055967 CRC64;
MALIDHLAPL RAHPGQRLTR GLDDTAIERL AKGHPDLVAV IEAAAAEHAR LQDEFSELLA
MDEAEQLRVV QSGYVNFYAD DAINPYIALA ARGPWVVTLK GAVLYDAGGY GMLGFGHTPA
AVLEAMARPQ VMANIMTPSL SQLRFDRALR KEIGHTRGGC PFAKFLCLNS GSESVGLAAR
IADINSKLMT DPDGRHAGRT IKRIVVKGSF HGRTERPALY SDSSRKSYQQ HLASYRGEDS
VIAIPPYDVD ALKQAFADAE TKGWFVEAVF LEPVMGEGDP GRSVPPAFYA AARELTRSHG
SLFLVDSIQA GLRAHGVLSI VDYPGFEGLD APDMETYSKA LNAAQYPLSV LAVNERAAGL
YRKGVYGNTM TTNPRALDVA CATLAQLTPQ VRQNIRKRGA EAVQKLQQLQ GELGGMITNV
QGTGLLFSCE LSPAFKCYGT GSTEEWLRQQ GLNVIHGGAN SLRFTPHFAI DGEELDLLVA
MVGKALREGP RISQAAAA
//
